ID A0A1A2VAA4_MYCSC Unreviewed; 432 AA.
AC A0A1A2VAA4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Aromatic-ring-hydroxylating dioxygenase subunit alpha {ECO:0000313|EMBL:OBH97661.1};
GN ORFNames=A5679_20660 {ECO:0000313|EMBL:OBH97661.1};
OS Mycobacterium scrofulaceum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1783 {ECO:0000313|EMBL:OBH97661.1, ECO:0000313|Proteomes:UP000092207};
RN [1] {ECO:0000313|EMBL:OBH97661.1, ECO:0000313|Proteomes:UP000092207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2838 {ECO:0000313|EMBL:OBH97661.1,
RC ECO:0000313|Proteomes:UP000092207};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBH97661.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LZJY01000274; OBH97661.1; -; Genomic_DNA.
DR RefSeq; WP_067307609.1; NZ_LZJY01000274.1.
DR AlphaFoldDB; A0A1A2VAA4; -.
DR Proteomes; UP000092207; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR CDD; cd03535; Rieske_RO_Alpha_NDO; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR043257; Rieske_N.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:OBH97661.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 25..138
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 432 AA; 48686 MW; 78AC57D3B929CB1E CRC64;
MVPAHIYNDA EVFALEKKRL FGRAWTFVAH ESEIPQDGDY VVRRVLDDSF IITRDSTGEV
RALFNMCLHR GMQVCRAEMG NASNFRCPYH GWTYRNDGQL TGLPFHREAY GGEDGFARKS
QSLLPAPNFA SYNGLLFISL DPNAEPLEEF LGDFAFYLDF YTKQSAGGVE VRGPQRWRIK
ANWKIGAENF AGDMYHTPHT HASIVDIGLF REPKAQKRKD GATYWAQRGG GTTYKLPPGG
FEERMRYVGY PDEMIGRIKG VWTSRQQRMV GEDGFMISAA TCFPNLSFVH NWPKVRDGHD
DETLPFISIR LWQPISENET EVCSWFAVDS AAPAQYKQDS YKAYLMCFGS TGMFEQDDVE
NWVSLTTTAG GSMARRLLLN SRMGLLSDGS PVVEPLTAEA FHGPGRAQVG YNEHNQRALL
SLWADYLQGA AP
//